{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim DK"],"funding":["Intramural NIH HHS","Chungbuk National University"],"pagination":["208-214"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9969741"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["567"],"pubmed_abstract":["The cell cycle is modulated by ubiquitin ligases, including CRL4, which facilitate degradation of the chromatin-bound substrates involved in DNA replication and chromosome segregation. One of the members of the CRL4 complex, RepID (DCAF14/PHIP), recognizes kinetochore-localizing BUB3, known as the CRL4 substrate, and recruits CRL4 to the chromatin/chromosome using the WD40 domain. Here, we show that the RepID WD40 domain provides different platforms to CRL4 and BUB3. Deletion of the H-box or exon 8 located in the RepID WD40 domain compromises the interaction between RepID and CRL4, whereas BUB3 interacts with the exon 1-2 region. Moreover, deletion mutants of other exons in the WD40 domain lost chromatin binding affinity. Structure prediction revealed that the RepID WD40 domain has two beta-propeller folds, linked by loops, which are possibly crucial for chromatin binding. These findings provide mechanistic insights into the space occupancy of the RepID WD40 domain to form a complex with CRL4, BUB3, or chromatin."],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["Molecular double clips within RepID WD40 domain control chromatin binding and CRL4-substrate assembly."],"pmcid":["PMC9969741"],"funding_grant_id":["Z01 BC010411"],"pubmed_authors":["Aladjem MI","Kim HK","Jang SM","Redon CE","Kim DK"],"additional_accession":[]},"is_claimable":false,"name":"Molecular double clips within RepID WD40 domain control chromatin binding and CRL4-substrate assembly.","description":"The cell cycle is modulated by ubiquitin ligases, including CRL4, which facilitate degradation of the chromatin-bound substrates involved in DNA replication and chromosome segregation. One of the members of the CRL4 complex, RepID (DCAF14/PHIP), recognizes kinetochore-localizing BUB3, known as the CRL4 substrate, and recruits CRL4 to the chromatin/chromosome using the WD40 domain. Here, we show that the RepID WD40 domain provides different platforms to CRL4 and BUB3. Deletion of the H-box or exon 8 located in the RepID WD40 domain compromises the interaction between RepID and CRL4, whereas BUB3 interacts with the exon 1-2 region. Moreover, deletion mutants of other exons in the WD40 domain lost chromatin binding affinity. Structure prediction revealed that the RepID WD40 domain has two beta-propeller folds, linked by loops, which are possibly crucial for chromatin binding. These findings provide mechanistic insights into the space occupancy of the RepID WD40 domain to form a complex with CRL4, BUB3, or chromatin.","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Aug","modification":"2025-04-04T00:35:51.903Z","creation":"2025-04-04T00:35:51.903Z"},"accession":"S-EPMC9969741","cross_references":{"pubmed":["34171797"],"doi":["10.1016/j.bbrc.2021.06.047"]}}